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Protein

Methyltransferase-like protein 2B

Gene

METTL2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probable S-adenosyl-L-methionine-dependent methyltransferase that mediates 3-methylcytidine modification of some tRNAs.1 Publication

GO - Molecular functioni

  • tRNA (cytosine) methyltransferase activity Source: UniProtKB

GO - Biological processi

  • tRNA methylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.268. 2681.
2.1.1.B109. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyltransferase-like protein 2B (EC:2.1.1.-)
Gene namesi
Name:METTL2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:18272. METTL2B.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134924546.

Polymorphism and mutation databases

BioMutaiMETTL2B.
DMDMi317373413.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 378377Methyltransferase-like protein 2BPRO_0000328847Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei4 – 41PhosphoserineCombined sources
Modified residuei154 – 1541PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ6P1Q9.
MaxQBiQ6P1Q9.
PaxDbiQ6P1Q9.
PeptideAtlasiQ6P1Q9.
PRIDEiQ6P1Q9.

PTM databases

iPTMnetiQ6P1Q9.
PhosphoSiteiQ6P1Q9.

Expressioni

Gene expression databases

BgeeiQ6P1Q9.
CleanExiHS_METTL2B.
ExpressionAtlasiQ6P1Q9. baseline and differential.
GenevisibleiQ6P1Q9. HS.

Interactioni

Protein-protein interaction databases

BioGridi120910. 7 interactions.
IntActiQ6P1Q9. 1 interaction.
STRINGi9606.ENSP00000262432.

Structurei

3D structure databases

ProteinModelPortaliQ6P1Q9.
SMRiQ6P1Q9. Positions 182-345.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2361. Eukaryota.
ENOG410YAN4. LUCA.
GeneTreeiENSGT00520000055554.
HOGENOMiHOG000182278.
HOVERGENiHBG075344.
InParanoidiQ6P1Q9.
OMAiEHKTQTP.
PhylomeDBiQ6P1Q9.
TreeFamiTF323232.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR026113. MeTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR22809. PTHR22809. 2 hits.
PIRSFiPIRSF037755. Mettl2_prd. 1 hit.
SUPFAMiSSF53335. SSF53335. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6P1Q9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGSYPEGAP AILADKRQQF GSRFLSDPAR VFHHNAWDNV EWSEEQAAAA
60 70 80 90 100
ERKVQENSIQ RVCQEKQVDY EINAHKYWND FYKIHENGFF KDRHWLFTEF
110 120 130 140 150
PELAPSQNQN HLKDWFLENK SEVCECRNNE DGPGLIMEEQ HKCSSKSLEH
160 170 180 190 200
KTQTPPVEEN VTQKISDLEI CADEFPGSSA TYRILEVGCG VGNTVFPILQ
210 220 230 240 250
TNNDPGLFVY CCDFSSTAIE LVQTNSEYDP SRCFAFVHDL CDEEKSYPVP
260 270 280 290 300
KGSLDIIILI FVLSAVVPDK MQKAINRLSR LLKPGGMVLL RDYGRYDMAQ
310 320 330 340 350
LRFKKGQCLS GNFYVRGDGT RVYFFTQEEL DTLFTTAGLE KVQNLVDRRL
360 370
QVNRGKQLTM YRVWIQCKYC KPLLSSTS
Note: No experimental confirmation available.
Length:378
Mass (Da):43,426
Last modified:January 11, 2011 - v3
Checksum:iA9719EF1074BA011
GO
Isoform 2 (identifier: Q6P1Q9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-67: MAGSYPEGAPAILADKRQQFGSRFLSDPARVFHHNAWDNVEWSEEQAAAAERKVQENSIQRVCQEKQ → MP

Show »
Length:313
Mass (Da):36,057
Checksum:i9A7C6CE35B445F0D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681V → I.1 Publication
Corresponds to variant rs2288557 [ dbSNP | Ensembl ].
VAR_059465
Natural varianti124 – 1241C → R.
Corresponds to variant rs2896399 [ dbSNP | Ensembl ].
VAR_042547
Natural varianti129 – 1291N → H.
Corresponds to variant rs2023329 [ dbSNP | Ensembl ].
VAR_042548
Natural varianti169 – 1691E → K.
Corresponds to variant rs1065267 [ dbSNP | Ensembl ].
VAR_042549
Natural varianti266 – 2661V → I.2 Publications
Corresponds to variant rs2562741 [ dbSNP | Ensembl ].
VAR_042550

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6767MAGSY…CQEKQ → MP in isoform 2. 2 PublicationsVSP_032816Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002212 mRNA. Translation: BAA92136.1.
AK302775 mRNA. Translation: BAG63980.1.
AC010655 Genomic DNA. No translation available.
AC090114 Genomic DNA. No translation available.
BC064929 mRNA. Translation: AAH64929.1.
BC107586 mRNA. Translation: AAI07587.1.
BC121115 mRNA. Translation: AAI21116.1.
BC121116 mRNA. Translation: AAI21117.1.
CCDSiCCDS5803.2. [Q6P1Q9-1]
RefSeqiNP_060866.2. NM_018396.2. [Q6P1Q9-1]
UniGeneiHs.433213.

Genome annotation databases

EnsembliENST00000262432; ENSP00000262432; ENSG00000165055. [Q6P1Q9-1]
ENST00000480046; ENSP00000418402; ENSG00000165055. [Q6P1Q9-2]
GeneIDi55798.
KEGGihsa:55798.
UCSCiuc003vnf.3. human. [Q6P1Q9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002212 mRNA. Translation: BAA92136.1.
AK302775 mRNA. Translation: BAG63980.1.
AC010655 Genomic DNA. No translation available.
AC090114 Genomic DNA. No translation available.
BC064929 mRNA. Translation: AAH64929.1.
BC107586 mRNA. Translation: AAI07587.1.
BC121115 mRNA. Translation: AAI21116.1.
BC121116 mRNA. Translation: AAI21117.1.
CCDSiCCDS5803.2. [Q6P1Q9-1]
RefSeqiNP_060866.2. NM_018396.2. [Q6P1Q9-1]
UniGeneiHs.433213.

3D structure databases

ProteinModelPortaliQ6P1Q9.
SMRiQ6P1Q9. Positions 182-345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120910. 7 interactions.
IntActiQ6P1Q9. 1 interaction.
STRINGi9606.ENSP00000262432.

PTM databases

iPTMnetiQ6P1Q9.
PhosphoSiteiQ6P1Q9.

Polymorphism and mutation databases

BioMutaiMETTL2B.
DMDMi317373413.

Proteomic databases

EPDiQ6P1Q9.
MaxQBiQ6P1Q9.
PaxDbiQ6P1Q9.
PeptideAtlasiQ6P1Q9.
PRIDEiQ6P1Q9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262432; ENSP00000262432; ENSG00000165055. [Q6P1Q9-1]
ENST00000480046; ENSP00000418402; ENSG00000165055. [Q6P1Q9-2]
GeneIDi55798.
KEGGihsa:55798.
UCSCiuc003vnf.3. human. [Q6P1Q9-1]

Organism-specific databases

CTDi55798.
GeneCardsiMETTL2B.
HGNCiHGNC:18272. METTL2B.
neXtProtiNX_Q6P1Q9.
PharmGKBiPA134924546.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2361. Eukaryota.
ENOG410YAN4. LUCA.
GeneTreeiENSGT00520000055554.
HOGENOMiHOG000182278.
HOVERGENiHBG075344.
InParanoidiQ6P1Q9.
OMAiEHKTQTP.
PhylomeDBiQ6P1Q9.
TreeFamiTF323232.

Enzyme and pathway databases

BRENDAi2.1.1.268. 2681.
2.1.1.B109. 2681.

Miscellaneous databases

GeneWikiiMETTL2B.
GenomeRNAii55798.
PROiQ6P1Q9.

Gene expression databases

BgeeiQ6P1Q9.
CleanExiHS_METTL2B.
ExpressionAtlasiQ6P1Q9. baseline and differential.
GenevisibleiQ6P1Q9. HS.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR026113. MeTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR22809. PTHR22809. 2 hits.
PIRSFiPIRSF037755. Mettl2_prd. 1 hit.
SUPFAMiSSF53335. SSF53335. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ILE-266.
    Tissue: Retinoblastoma and Testis.
  2. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-378 (ISOFORM 1), VARIANTS ILE-68 AND ILE-266.
    Tissue: Eye.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine at position 32 of tRNAs in Saccharomyces cerevisiae."
    Noma A., Yi S., Katoh T., Takai Y., Suzuki T., Suzuki T.
    RNA 17:1111-1119(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND THR-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiMET2B_HUMAN
AccessioniPrimary (citable) accession number: Q6P1Q9
Secondary accession number(s): B4DZ68, Q0IJ54, Q3B7J1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: January 11, 2011
Last modified: July 6, 2016
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.